Flagellar Stators Activate a Diguanylate Cyclase To Inhibit Flagellar Stators

J Bacteriol. 2019 Aug 22;201(18):e00186-19. doi: 10.1128/JB.00186-19. Print 2019 Sep 15.

Abstract

The bacterial secondary metabolite cyclic di-GMP is a widespread, cytoplasmic signal that promotes a physiological transition in which motility is inhibited and biofilm formation is activated. A paper published in this issue (A. E. Baker, S. S. Webster, A. Diepold, S. L. Kuchma, E. Bordeleau, et al., J Bacteriol 201:e00741-18, 2019, https://doi.org/10.1128/JB.00741-18) makes an important connection between cyclic di-GMP and flagellar components. They show that stator units, which normally interact with the flagellum to power rotation, can alternatively interact with and activate an enzyme that synthesizes cyclic di-GMP in Pseudomonas aeruginosa. Moreover, the same stator units are also the target of cyclic-di-GMP-dependent inhibition such that the more the stators are inhibited, the more cyclic di-GMP is made. The resulting positive-feedback loop not only inhibits motility but also may initiate and stabilize biofilm formation.

MeSH terms

  • Bacterial Proteins / metabolism*
  • Biofilms / growth & development
  • Cyclic GMP / analogs & derivatives
  • Cyclic GMP / metabolism
  • Escherichia coli Proteins / metabolism*
  • Flagella / metabolism*
  • Gene Expression Regulation, Bacterial / physiology
  • Phosphorus-Oxygen Lyases / metabolism*
  • Pseudomonas aeruginosa / metabolism

Substances

  • Bacterial Proteins
  • Escherichia coli Proteins
  • bis(3',5')-cyclic diguanylic acid
  • Phosphorus-Oxygen Lyases
  • diguanylate cyclase
  • Cyclic GMP